Structural and functional characterisation of a conserved archaeal RadA paralog with antirecombinase activity.

@article{McRobbie2009StructuralAF,
  title={Structural and functional characterisation of a conserved archaeal RadA paralog with antirecombinase activity.},
  author={Anne-Marie McRobbie and Lester G. Carter and Melina Kerou and Huanting Liu and Stephen A. McMahon and K A Johnson and Muse Oke and James H. Naismith and Malcolm F White},
  journal={Journal of molecular biology},
  year={2009},
  volume={389 4},
  pages={661-73}
}
DNA recombinases (RecA in bacteria, Rad51 in eukarya and RadA in archaea) catalyse strand exchange between homologous DNA molecules, the central reaction of homologous recombination, and are among the most conserved DNA repair proteins known. RecA is the sole protein responsible for this reaction in bacteria, whereas there are several Rad51 paralogs that cooperate to catalyse strand exchange in eukaryotes. All archaea have at least one (and as many as four) RadA paralog, but their function… CONTINUE READING

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( RecA in bacteria , Rad51 in eukarya and RadA in archaea ) catalyse strand exchange between homologous DNA molecules , the central reaction of homologous recombination , and are among the most conserved DNA repair proteins known .
( RecA in bacteria , Rad51 in eukarya and RadA in archaea ) catalyse strand exchange between homologous DNA molecules , the central reaction of homologous recombination , and are among the most conserved DNA repair proteins known .
( RecA in bacteria , Rad51 in eukarya and RadA in archaea ) catalyse strand exchange between homologous DNA molecules , the central reaction of homologous recombination , and are among the most conserved DNA repair proteins known .
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